VP2_POVMA
ID VP2_POVMA Reviewed; 319 AA.
AC P03096; Q85070;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 98.
DE RecName: Full=Minor capsid protein VP2;
DE AltName: Full=Minor structural protein VP2;
OS Murine polyomavirus (strain A2) (MPyV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Alphapolyomavirus.
OX NCBI_TaxID=10636;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6243401; DOI=10.1038/283445a0;
RA Soeda E., Arrand J.R., Smolar N., Walsh J.E., Griffin B.E.;
RT "Coding potential and regulatory signals of the polyoma virus genome.";
RL Nature 283:445-453(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6251236; DOI=10.1128/jvi.33.2.606-618.1980;
RA Arrand J.R., Soeda E., Walsh J.E., Smolar N., Griffin B.E.;
RT "Polyoma virus DNA: Sequence from the late region that specifies the leader
RT sequence for late mRNA and codes for VP2, VP3, and the N-terminus of VP1.";
RL J. Virol. 33:606-618(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 283-319.
RX PubMed=6251237; DOI=10.1128/jvi.33.2.619-630.1980;
RA Soeda E., Arrand J.R., Griffin B.E.;
RT "Polyoma virus DNA: complete nucleotide sequence of the gene which codes
RT for polyoma virus capsid protein VP1 and overlaps the VP2/VP3 genes.";
RL J. Virol. 33:619-630(1980).
RN [4]
RP MYRISTOYLATION AT GLY-2, AND SUBCELLULAR LOCATION.
RX PubMed=3031509; DOI=10.1038/326619a0;
RA Streuli C.H., Griffin B.E.;
RT "Myristic acid is coupled to a structural protein of polyoma virus and
RT SV40.";
RL Nature 326:619-622(1987).
RN [5]
RP REVIEW.
RX PubMed=19157478; DOI=10.1016/j.virol.2008.12.021;
RA Neu U., Stehle T., Atwood W.J.;
RT "The Polyomaviridae: Contributions of virus structure to our understanding
RT of virus receptors and infectious entry.";
RL Virology 384:389-399(2009).
CC -!- FUNCTION: Isoform VP2 is a structural protein that resides within the
CC core of the capsid surrounded by 72 VP1 pentamers. Participates in host
CC cell receptor binding together with VP1. Following virus endocytosis
CC and trafficking to the endoplasmic reticulum, VP2 and VP3 form
CC oligomers and integrate into the endoplasmic reticulum membrane.
CC Heterooligomer VP2-VP3 may create a viroporin for transporting the
CC viral genome across the endoplasmic reticulum membrane to the
CC cytoplasm. Nuclear entry of the viral DNA involves the selective
CC exposure and importin recognition of VP2 or Vp3 nuclear localization
CC signal (shared C-terminus). Plays a role in virion assembly within the
CC nucleus in particular through a DNA-binding domain located in the C-
CC terminal region. A N-terminal myristoylation suggests a scaffold
CC function for virion assembly (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Isoform VP3]: Structural protein that resides within the
CC core of the capsid surrounded by 72 VP1 pentamers. Following virus
CC endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3
CC form oligomers and integrate into the endoplasmic reticulum membrane.
CC Heterooligomer VP2-VP3 may create a viroporin for transporting the
CC viral genome across the endoplasmic reticulum membrane to the
CC cytoplasm. Nuclear entry of the viral DNA involves the selective
CC exposure and importin recognition of VP2 or Vp3 nuclear localization
CC signal (shared C-terminus). Isoform VP3 plays a role in virion assembly
CC within the nucleus (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Isoform VP2 forms homooligomers, and heterooligomers with VP3
CC in the endoplasmic reticulum membrane. Isoform VP2 interacts (via D1
CC domain) with VP1. Isoform VP3 interacts (via D1 domain) with VP1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host
CC endoplasmic reticulum. Host endoplasmic reticulum membrane
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host
CC endoplasmic reticulum. Host endoplasmic reticulum membrane
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P03096-1; Sequence=Displayed;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P03096-2; Sequence=VSP_018922;
CC Name=VP1;
CC IsoId=P03090-1; Sequence=External;
CC -!- MISCELLANEOUS: [Isoform VP2]: Produced by alternative splicing of the
CC late mRNA.
CC -!- MISCELLANEOUS: [Isoform VP3]: Produced by alternative initiation at
CC Met-116 of isoform VP2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family.
CC {ECO:0000305}.
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DR EMBL; J02288; AAB59903.1; -; Genomic_DNA.
DR EMBL; J02288; AAB59904.1; -; Genomic_DNA.
DR PIR; A03635; VVVP2.
DR DIP; DIP-1089N; -.
DR IntAct; P03096; 2.
DR MINT; P03096; -.
DR iPTMnet; P03096; -.
DR PRIDE; P03096; -.
DR Proteomes; UP000008479; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR InterPro; IPR001070; Polyoma_coat_VP2.
DR Pfam; PF00761; Polyoma_coat2; 1.
DR PIRSF; PIRSF003377; Polyoma_coat2; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Alternative splicing; Capsid protein; DNA-binding;
KW Host endoplasmic reticulum; Host membrane; Host nucleus; Late protein;
KW Lipoprotein; Membrane; Myristate; Reference proteome; Transmembrane;
KW Transmembrane helix; Viral penetration into host nucleus; Virion;
KW Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT CHAIN 2..319
FT /note="Minor capsid protein VP2"
FT /id="PRO_0000039217"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 266..301
FT /note="D1"
FT /evidence="ECO:0000250"
FT REGION 306..319
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT MOTIF 311..319
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000269|PubMed:3031509"
FT VAR_SEQ 1..115
FT /note="Missing (in isoform VP3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018922"
SQ SEQUENCE 319 AA; 34801 MW; F7168DBCC7A8654C CRC64;
MGAALTILVD LIEGLAEVST LTGLSAEAIL SGEALAALDG EITALTLEGV MSSETALATM
GISEEVYGFV STVPVFVSRT AGAIWLMQTV QGASTISLGI QRYLHNEEVP TVNRNMALIP
WRDPALLDIY FPGVNQFAHA LNVVHDWGHG LLHSVGRYVW QMVVQETQHR LEGAVRELTV
RQTHTFLDGL ARLLENTRWV VSNAPQSAID AINRGASSAS SGYSSLSDYY RQLGLNPPQR
RALFNRIEGS MGNGGPTPAA HIQDESGEVI KFYQAQVVSH QRVTPDWMLP LILGLYGDIT
PTWATVIEED GPQKKKRRL
